title: Heat shock proteins bind calcitonin.
abstract: We have demonstrated two heat shock proteins (HSP's) in the human placenta that specifically bind calcitonin. Binding specificity was shown by ligand-affinity chromatography and by competitive binding studies. The HSP's were identified by Western analysis and by amino acid sequence. Our observations are consistent with the hypothesis that HSP's may function by binding and interacting with cellular proteins and peptides during their biogenesis. This interaction may both depend upon and produce conformational changes in these ligands during their intracellular processing. Additionally, HSP-peptide hormone interactions may confound studies designed to investigate classical receptor-hormone interactions.
authors.affiliation: Department of Medicine, University of California, La Jolla.
authors.forename: R C
authors.initials: RC
authors.lastname: Dana
authors.forename: W J
authors.initials: WJ
authors.lastname: Welch
authors.forename: L J
authors.initials: LJ
authors.lastname: Deftos
mesh_terms: D000595:Amino Acid Sequence; D001667:Binding, Competitive; D002116:Calcitonin / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008970:Molecular Weight; D010920:Placenta / Q000378:metabolism; D011257:Pregnancy Proteins / Q000378:metabolism
chemical_list: D006360:Heat-Shock Proteins; D011257:Pregnancy Proteins; D002116:Calcitonin